Structural Basis for Specific Substrate Recognition by the Chloroplast Signal Recognition Particle Protein cpSRP43

Stengel, Katharina; Holdermann, I.; Cain, Peter; Robinson, Colin; Wild, Klemens; Sinning, Irmgard

doi:10.1126/science.1158640

Cited by 81 publications

(146 citation statements)

References 34 publications

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“…As shown in Figure 6e,f, similar results were obtained using this system. As expected, cpSRP43 interacted with the pLHCP 163 − 206 region, which contains the L18 region 18,19 (Fig. 6e).…”

Section: Cellular Localization Of Ltdsupporting

confidence: 82%

“…3b). A parallel set of protein overlay experiments using ltd stromal proteins showed the interaction between cpSRP54 and cpSRP43, which is consistent with the formation of a stable cpSRP43 and cpSRP54 heterodimer 19,36 . However, cpSRP43 has also been suggested to be a dimer through gel filtration and chemical cross-linking experiments 20 .…”

Section: Cellular Localization Of Ltdsupporting

confidence: 62%

“…As cpSRP43 specifically recognizes the L18 region in LHCP 18,19 , we next investigated whether LTD also recognizes a specific region in LHCP. An alignment of the amino-acid sequences of LHCP (Lhcb1-6 and Lhca1-4) revealed several strictly conserved amino-acid regions ( Supplementary Fig.…”

Section: Cellular Localization Of Ltdmentioning

confidence: 99%

“…The ankyrin domain of cpSRP43 interacts with a conserved L18 region between the second and third transmembrane domains of LHCP 18,19 . Targeting of LHCP to the membrane also requires the chloroplast SRP receptor homologue cpFtsY and GTP 20 .…”

mentioning

confidence: 99%

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LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway

Ouyang

et al. 2011

Nat Commun

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Higher plants require chloroplasts for essential functions in photosynthesis and other important physiological processes, such as sugar, lipid and amino-acid biosynthesis. most chloroplast proteins are nuclear-encoded proteins that are synthesized in the cytosol as precursors, and imported into chloroplasts by protein translocases in the outer and inner chloroplast envelope. The imported chloroplast proteins are then translocated into or across the thylakoid membrane by four distinct pathways. However, the mechanisms by which the imported nuclear-encoded proteins are delivered to these pathways remain largely unknown. Here we show that an Arabidopsis ankyrin protein, LTD (mutation of which causes the light-harvesting chlorophyllbinding protein translocation defect), is localized in the chloroplast and using yeast two-hybrid screens demonstrate that LTD interacts with both proteins from the signal recognition particle (sRP) pathway and the inner chloroplast envelope. our study shows that LTD is essential for the import of light-harvesting chlorophyll-binding proteins and subsequent routing of these proteins to the chloroplast sRP-dependent pathway.

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“…As shown in Figure 6e,f, similar results were obtained using this system. As expected, cpSRP43 interacted with the pLHCP 163 − 206 region, which contains the L18 region 18,19 (Fig. 6e).…”

Section: Cellular Localization Of Ltdsupporting

confidence: 82%

Section: Cellular Localization Of Ltdsupporting

confidence: 62%

Section: Cellular Localization Of Ltdmentioning

confidence: 99%

mentioning

confidence: 99%

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LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway

Ouyang

et al. 2011

Nat Commun

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“…An analogous situation is seen in chloroplast SRP, where a single protein performs the function of this otherwise ubiquituous RNP complex (98).…”

Section: Exceptions To the Rule: Uncommon Sources For Rnase P/mrp Funmentioning

confidence: 90%

Ribonucleases P/MRP and the Expanding Ribonucleoprotein World

et al. 2012

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SummaryOne of the hallmarks of life is the widespread use of certain essential ribozymes. The ubiquitous ribonuclease P (RNase P) and eukaryotic RNase MRP are essential complexes where a structured, noncoding RNA acts in catalysis. Recent discoveries have elucidated the three-dimensional structure of the ancestral ribonucleoprotein complex, suggested the possibility of a proteinonly composition in organelles, and even noted the absence of RNase P in a non-free-living organism. With respect to these last two findings, import mechanisms for RNases P/MRP into mitochondria have been demonstrated, and RNase P is present in organisms with some of the smallest known genomes. Together, these results have led to an ongoing debate regarding the precise definition of how ''essential'' these ribozymes truly are. IUBMBIUBMB Life, 64(6): [521][522][523][524][525][526][527][528] 2012

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Simultaneous CAS9 editing of cpSRP43, LHCA6, and LHCA7 in Picochlorum celeri lowers chlorophyll levels and improves biomass productivity

Krishnan,

Cano,

Karns

et al. 2023

Plant Direct

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High cellular pigment levels in dense microalgal cultures contribute to excess light absorption. To improve photosynthetic yields in the marine microalga Picochlorum celeri, CAS9 gene editing was used to target the molecular chaperone cpSRP43. Depigmented strains (>50% lower chlorophyll) were generated, with proteomics showing attenuated levels of most light harvesting complex (LHC) proteins. Gene editing generated two types of cpSRP43 transformants with distinct lower pigment phenotypes: (i) a transformant (Δsrp43) with both cpSRP43 diploid alleles modified to encode non‐functional polypeptides and (ii) a transformant (STR30309) with a 3 nt in‐frame insertion in one allele at the CAS9 cut site (non‐functional second allele), leading to expression of a modified cpSRP43. STR30309 has more chlorophyll than Δsrp43 but substantially less than wild type. To further decrease light absorption by photosystem I in STR30309, CAS9 editing was used to stack in disruptions of both LHCA6 and LHCA7 to generate STR30843, which has higher (5–24%) productivities relative to wild type in solar‐simulating bioreactors. Maximal productivities required frequent partial harvests throughout the day. For STR30843, exemplary diel bioreactor yields of ~50 g m−2 day−1 were attained. Our results demonstrate diel productivity gains in P. celeri by lowering pigment levels.

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Structural Basis for Specific Substrate Recognition by the Chloroplast Signal Recognition Particle Protein cpSRP43

Cited by 81 publications

References 34 publications

LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway

LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway

Ribonucleases P/MRP and the Expanding Ribonucleoprotein World

Simultaneous CAS9 editing of cpSRP43, LHCA6, and LHCA7 in Picochlorum celeri lowers chlorophyll levels and improves biomass productivity

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